Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2MU7

Shortening and modifying the 1513 MSP-1 peptide's alpha-helical region induces protection against malaria

Summary for 2MU7
Entry DOI10.2210/pdb2mu7/pdb
Related2MU8
NMR InformationBMRB: 25201
Descriptor1513 MSP-1 peptide (1 entity in total)
Functional Keywordsmsp-1 protein, cell invasion
Biological sourcePlasmodium falciparum
Total number of polymer chains1
Total formula weight2162.42
Authors
Espejo, F.,Bermudez, A.,Torres, E.,Urquiza, M.,Rodriguez, R.,Lopez, Y.,Patarroyo, M. (deposition date: 2014-09-04, release date: 2014-11-12, Last modification date: 2024-05-15)
Primary citationEspejo, F.,Bermudez, A.,Torres, E.,Urquiza, M.,Rodriguez, R.,Lopez, Y.,Patarroyo, M.E.
Shortening and modifying the 1513 MSP-1 peptide's alpha-helical region induces protection against malaria.
Biochem.Biophys.Res.Commun., 315:418-427, 2004
Cited by
PubMed Abstract: Immunogenic and protective peptide sequences are of prime importance in the search for an anti-malarial vaccine. The MSP-1 conserved and semi-conserved sequences have been shown to contain red blood cell (RBC) membrane high affinity binding peptides (HABP). HABP 1513 sequence ((42)GYSLFQKEKMVLNEGTSGTA(61)), from this protein's N-terminal, has been shown to possess a T-epitope; however, it did not induce a humoral immune response or complete protection when evaluated in Aotus monkeys. Analogue peptides with critical binding residues replaced by amino acids with similar mass but different charge were synthesised and tested for immunogenicity and protectivity in monkey. NMR studies correlated structural behaviour with biological function. Non-immunogenic and non-protective 1513 native peptide presented a helical fragment between residues L(4) and E(14). C-terminal, 5-residue-shorter, non-immunogenic, non-protective peptide 17894 contained an alpha-helix from Q(6) to L(12) residues. Immunogenic and protective peptide 13946 presented a shorter alpha-helix between K(7) to N(13) residues. These data suggest that changing certain residues permits better peptide fit within the MHC class II-peptide-TCR complex, thus activating the immune system and inducing a protective immune response.
PubMed: 14766224
DOI: 10.1016/j.bbrc.2004.01.072
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

243911

数据于2025-10-29公开中

PDB statisticsPDBj update infoContact PDBjnumon